ID   END8_ECOL5              Reviewed;         263 AA.
AC   Q0TJX8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Endonuclease 8;
DE   AltName: Full=Endonuclease VIII;
DE   AltName: Full=DNA glycosylase/AP lyase Nei;
DE            EC=3.2.2.-;
DE            EC=4.2.99.18;
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei;
GN   Name=nei; OrderedLocusNames=ECP_0727;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has a preference for
CC       oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil
CC       and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase
CC       activity and introduces nicks in the DNA strand. Cleaves the DNA
CC       backbone by beta-delta elimination to generate a single-strand
CC       break at the site of the removed base with both 3'- and 5'-
CC       phosphates (By similarity).
CC   -!- CATALYTIC ACTIVITY: Removes damaged bases from DNA, leaving an
CC       abasic site.
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the FPG family.
CC   -!- SIMILARITY: Contains 1 FPG-type zinc finger.
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DR   EMBL; CP000247; ABG68753.1; -; Genomic_DNA.
DR   RefSeq; YP_668652.1; -.
DR   SMR; Q0TJX8; 2-263.
DR   GeneID; 4191409; -.
DR   GenomeReviews; CP000247_GR; ECP_0727.
DR   KEGG; ecp:ECP_0727; -.
DR   HOGENOM; Q0TJX8; -.
DR   OMA; Q0TJX8; RSDFRVP.
DR   BioCyc; ECOL362663:ECP_0727-MON; -.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0000703; F:oxidized pyrimidine base lesion DNA N-glyco...; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   HAMAP; MF_01253; -; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR000214; DNA_glyclase/AP_lyase_Znf_dom.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR012319; DNA_glycosylase/AP_lyase_cat.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   ProDom; PD003680; Fapy_DNA_glyco; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS01242; ZF_FPG_1; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
KW   Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    263       Endonuclease 8.
FT                                /FTId=PRO_1000067202.
FT   ZN_FING     229    263       FPG-type.
FT   ACT_SITE      2      2       Schiff-base intermediate with DNA (By
FT                                similarity).
FT   ACT_SITE      3      3       Proton donor (By similarity).
FT   ACT_SITE     53     53       Proton donor; for beta-elimination
FT                                activity (By similarity).
FT   ACT_SITE    253    253       Proton donor; for delta-elimination
FT                                activity (By similarity).
FT   BINDING      70     70       DNA (By similarity).
FT   BINDING     125    125       DNA (By similarity).
FT   BINDING     169    169       DNA (By similarity).
SQ   SEQUENCE   263 AA;  29811 MW;  0D8EFFCBC8DD1A27 CRC64;
     MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKSYQSRL IGQHVTHVET RGKALLTHFS
     NDLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT ILLYSASDIE MLTPEQLTTH
     PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG
     LTGNHKAKDL NAAQLDALAH ALLDIPRLSY ATRGQVDENK YHGALFRFKV FHRDGEPCER
     CGGIIEKTTL SSRPFYWCPG CQH
//